{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,11]],"date-time":"2025-11-11T13:20:25Z","timestamp":1762867225990,"version":"3.37.3"},"reference-count":49,"publisher":"Springer Science and Business Media LLC","issue":"3","license":[{"start":{"date-parts":[[2017,9,20]],"date-time":"2017-09-20T00:00:00Z","timestamp":1505865600000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"funder":[{"DOI":"10.13039\/501100004731","name":"Natural Science Foundation of Zhejiang Province","doi-asserted-by":"publisher","award":["No. LY15B010002"],"award-info":[{"award-number":["No. LY15B010002"]}],"id":[{"id":"10.13039\/501100004731","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Appl Biochem Biotechnol"],"published-print":{"date-parts":[[2018,3]]},"DOI":"10.1007\/s12010-017-2607-0","type":"journal-article","created":{"date-parts":[[2017,9,20]],"date-time":"2017-09-20T05:58:52Z","timestamp":1505887132000},"page":"1009-1023","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":15,"title":["Improved Biodegradation of Synthetic Azo Dye by Anionic Cross-Linking of Chloroperoxidase on ZnO\/SiO2 Nanocomposite Support"],"prefix":"10.1007","volume":"184","author":[{"given":"Xinyu","family":"Jin","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Saisai","family":"Li","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nengbing","family":"Long","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3514-0455","authenticated-orcid":false,"given":"Ruifeng","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2017,9,20]]},"reference":[{"key":"2607_CR1","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1023\/A:1010306114286","volume":"23","author":"J-S Chang","year":"2001","unstructured":"Chang, J.-S., & Lin, C.-Y. (2001). Decolorization kinetics of a recombinant Escherichia coli strain harboring azo-dye-decolorizing determinants from Rhodococcus sp. Biotechnology Letters, 23, 631\u2013636.","journal-title":"Biotechnology Letters"},{"key":"2607_CR2","doi-asserted-by":"crossref","first-page":"9049","DOI":"10.1016\/j.biortech.2010.07.034","volume":"101","author":"SA Ong","year":"2010","unstructured":"Ong, S. A., Uchiyama, K., Inadama, D., Ishida, Y., & Yamagiwa, K. (2010). Treatment of azo dye acid Orange 7 containing wastewater using up-flow constructed wetland with and without supplementary aeration. Bioresource Technology, 101, 9049\u20139057.","journal-title":"Bioresource Technology"},{"key":"2607_CR3","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/S0143-7208(03)00064-0","volume":"58","author":"C Pearce","year":"2003","unstructured":"Pearce, C. (2003). The removal of colour from textile wastewater using whole bacterial cells: a review. Dyes and Pigments, 58, 179\u2013196.","journal-title":"Dyes and Pigments"},{"key":"2607_CR4","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0926-3373(03)00228-5","volume":"46","author":"E Torres","year":"2003","unstructured":"Torres, E., Bustos-Jaimes, I., & Le Borgne, S. (2003). Potential use of oxidative enzymes for the detoxification of organic pollutants. Applied Catalysis B: Environmental, 46, 1\u201315.","journal-title":"Applied Catalysis B: Environmental"},{"key":"2607_CR5","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1016\/j.chemosphere.2004.12.017","volume":"60","author":"S Akhtar","year":"2005","unstructured":"Akhtar, S., Khan, A. A., & Husain, Q. (2005). Potential of immobilized bitter gourd (Momordica charantia) peroxidases in the decolorization and removal of textile dyes from polluted wastewater and dyeing effluent. Chemosphere, 60, 291\u2013301.","journal-title":"Chemosphere"},{"key":"2607_CR6","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1080\/07388550600969936","volume":"26","author":"Q Husain","year":"2006","unstructured":"Husain, Q. (2006). Potential applications of the oxidoreductive enzymes in the decolorization and detoxification of textile and other synthetic dyes from polluted water: a review. Critical Reviews in Biotechnology, 26, 201\u2013221.","journal-title":"Critical Reviews in Biotechnology"},{"key":"2607_CR7","doi-asserted-by":"crossref","unstructured":"Haddaji, D., Bousselmi, L., Saadani, O., Nouairi, I., & Ghrabi-Gammar, Z. (2014). Enzymatic degradation of azo dyes using three macrophyte species: Arundo donax. Typha angustifoliaand Phragmites australis. Desalination and Water Treatment, 1\u201310.","DOI":"10.1080\/19443994.2014.884475"},{"key":"2607_CR8","doi-asserted-by":"crossref","first-page":"790","DOI":"10.1080\/00032719.2015.1081916","volume":"49","author":"A Akkaya","year":"2015","unstructured":"Akkaya, A., Erdogan Ozseker, E., & Akdogan, H. A. (2015). Degradation of dyes by laccase. Analytical Letters, 49, 790\u2013798.","journal-title":"Analytical Letters"},{"key":"2607_CR9","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1016\/j.enzmictec.2007.01.020","volume":"41","author":"X Cheng","year":"2007","unstructured":"Cheng, X., Jia, R., Li, P., Tu, S., Zhu, Q., Tang, W., et al. (2007). Purification of a new manganese peroxidase of the white-rot fungus Schizophyllum sp. F17, and decolorization of azo dyes by the enzyme. Enzyme and Microbial Technology, 41, 258\u2013264.","journal-title":"Enzyme and Microbial Technology"},{"key":"2607_CR10","doi-asserted-by":"crossref","first-page":"2131","DOI":"10.1007\/s12010-014-1158-x","volume":"174","author":"T Senthilvelan","year":"2014","unstructured":"Senthilvelan, T., Kanagaraj, J., & Panda, R. C. (2014). Enzyme-mediated bacterial biodegradation of an azo dye (C.I. Acid Blue 113): reuse of treated dye wastewater in post-tanning operations. Applied Biochemistry and Biotechnology, 174, 2131\u20132152.","journal-title":"Applied Biochemistry and Biotechnology"},{"key":"2607_CR11","doi-asserted-by":"crossref","first-page":"1748","DOI":"10.1016\/j.procbio.2015.07.009","volume":"50","author":"W Chen","year":"2015","unstructured":"Chen, W., Zheng, L., Jia, R., & Wang, N. (2015). Cloning and expression of a new manganese peroxidase from Irpex lacteus F17 and its application in decolorization of reactive black 5. Process Biochemistry, 50, 1748\u20131759.","journal-title":"Process Biochemistry"},{"key":"2607_CR12","doi-asserted-by":"crossref","first-page":"1529","DOI":"10.1007\/s12010-015-1674-3","volume":"176","author":"U Kalsoom","year":"2015","unstructured":"Kalsoom, U., Bhatti, H. N., & Asgher, M. (2015). Characterization of plant peroxidases and their potential for degradation of dyes: a review. Applied Biochemistry and Biotechnology, 176, 1529\u20131550.","journal-title":"Applied Biochemistry and Biotechnology"},{"key":"2607_CR13","doi-asserted-by":"crossref","first-page":"1199","DOI":"10.1016\/j.ibiod.2011.05.010","volume":"65","author":"HF Pajot","year":"2011","unstructured":"Pajot, H. F., Fari\u00f1a, J. I., & de Figueroa, L. I. C. (2011). Evidence on manganese peroxidase and tyrosinase expression during decolorization of textile industry dyes by Trichosporon akiyoshidainum. International Biodeterioration & Biodegradation, 65, 1199\u20131207.","journal-title":"International Biodeterioration & Biodegradation"},{"key":"2607_CR14","doi-asserted-by":"crossref","first-page":"716","DOI":"10.1007\/s12010-013-0377-x","volume":"171","author":"M Celebi","year":"2013","unstructured":"Celebi, M., Kaya, M. A., Altikatoglu, M., & Yildirim, H. (2013). Enzymatic decolorization of anthraquinone and diazo dyes using horseradish peroxidase enzyme immobilized onto various polysulfone supports. Applied Biochemistry and Biotechnology, 171, 716\u2013730.","journal-title":"Applied Biochemistry and Biotechnology"},{"key":"2607_CR15","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.abb.2016.02.026","volume":"596","author":"R Zhang","year":"2016","unstructured":"Zhang, R., He, Q., Huang, Y., & Wang, X. (2016). Spectroscopic and QM\/MM investigations of chloroperoxidase catalyzed degradation of orange G. Archives of Biochemistry and Biophysics, 596, 1\u20139.","journal-title":"Archives of Biochemistry and Biophysics"},{"key":"2607_CR16","doi-asserted-by":"crossref","first-page":"13572","DOI":"10.1021\/ie4007563","volume":"52","author":"X Li","year":"2013","unstructured":"Li, X., Zhang, J., Jiang, Y., Hu, M., Li, S., & Zhai, Q. (2013). Highly efficient biodecolorization\/degradation of Congo red and alizarin yellow R by chloroperoxidase from Caldariomyces fumago: catalytic mechanism and degradation pathway. Industrial & Engineering Chemistry Research, 52, 13572\u201313579.","journal-title":"Industrial & Engineering Chemistry Research"},{"key":"2607_CR17","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/j.micromeso.2005.04.008","volume":"83","author":"J Aburto","year":"2005","unstructured":"Aburto, J., Ayala, M., Bustos-Jaimes, I., Montiel, C., Terr\u00e9s, E., Dom\u00ednguez, J. M., et al. (2005). Stability and catalytic properties of chloroperoxidase immobilized on SBA-16 mesoporous materials. Microporous and Mesoporous Materials, 83, 193\u2013200.","journal-title":"Microporous and Mesoporous Materials"},{"key":"2607_CR18","unstructured":"Ayala M, Batista CV, Vazquez-Duhalt R. (2011). Heme destruction, the main molecular event during the peroxide-mediated inactivation of chloroperoxidase from Caldariomyces fumago. Journal of biological inorganic chemistry : JBIC: a publication of the Society of Biological. Inorganic Chemistry, 16, 63\u201368."},{"key":"2607_CR19","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1080\/10242420802393519","volume":"27","author":"DJ Leak","year":"2009","unstructured":"Leak, D. J., Sheldon, R. A., Woodley, J. M., & Adlercreutz, P. (2009). Biocatalysts for selective introduction of oxygen. Biocatalysis and Biotransformation, 27, 1\u201326.","journal-title":"Biocatalysis and Biotransformation"},{"key":"2607_CR20","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.apcata.2014.12.016","volume":"492","author":"L Matteis De","year":"2015","unstructured":"De Matteis, L., Germani, R., Mancini, M. V., Di Renzo, F., & Spreti, N. (2015). Encapsulation of chloroperoxidase in novel hybrid polysaccharide-silica biocomposites: catalytic efficiency, re-use and thermal stability. Applied Catalysis A: General, 492, 23\u201330.","journal-title":"Applied Catalysis A: General"},{"issue":"116","key":"2607_CR21","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.molcatb.2015.02.014","volume":"5","author":"FA Mu\u00f1oz-Guerrero","year":"2015","unstructured":"Mu\u00f1oz-Guerrero, F. A., \u00c1guila, S., Vazquez-Duhalt, R., & Alderete, J. B. (2015). Enhancement of operational stability of chloroperoxidase from Caldariomyces fumago by immobilization onto mesoporous supports and the use of co-solvents. Journal of Molecular Catalysis B: Enzymatic, 5(116), 1\u20138.","journal-title":"Journal of Molecular Catalysis B: Enzymatic"},{"key":"2607_CR22","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1016\/j.molcatb.2012.04.010","volume":"84","author":"M Pe\u0161i\u0107","year":"2012","unstructured":"Pe\u0161i\u0107, M., L\u00f3pez, C., \u00c1lvaro, G., & L\u00f3pez-Sant\u00edn, J. (2012). A novel immobilized chloroperoxidase biocatalyst with improved stability for the oxidation of amino alcohols to amino aldehydes. Journal of Molecular Catalysis B: Enzymatic, 84, 144\u2013151.","journal-title":"Journal of Molecular Catalysis B: Enzymatic"},{"key":"2607_CR23","doi-asserted-by":"crossref","first-page":"1269","DOI":"10.1007\/s10529-009-0009-2","volume":"31","author":"LH Zhang","year":"2009","unstructured":"Zhang, L. H., Bai, C. H., Wang, Y. S., Jiang, Y. C., Hu, M. C., Li, S. N., et al. (2009). Improvement of chloroperoxidase stability by covalent immobilization on chitosan membranes. Biotechnology Letters, 31, 1269\u20131272.","journal-title":"Biotechnology Letters"},{"key":"2607_CR24","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1016\/j.bej.2007.06.018","volume":"38","author":"G Bayramo\u011flu","year":"2008","unstructured":"Bayramo\u011flu, G., Kiralp, S., Yilmaz, M., Toppare, L., & Ar\u0131ca, M. Y. (2008). Covalent immobilization of chloroperoxidase onto magnetic beads: catalytic properties and stability. Biochemical Engineering Journal, 38, 180\u2013188.","journal-title":"Biochemical Engineering Journal"},{"key":"2607_CR25","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1016\/j.biortech.2010.08.056","volume":"102","author":"G Bayramoglu","year":"2011","unstructured":"Bayramoglu, G., Altintas, B., Yilmaz, M., & Arica, M. Y. (2011). Immobilization of chloroperoxidase onto highly hydrophilic polyethylene chains via bio-conjugation: catalytic properties and stabilities. Bioresource Technology, 102, 475\u2013482.","journal-title":"Bioresource Technology"},{"key":"2607_CR26","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.molcatb.2013.07.011","volume":"97","author":"L Matteis De","year":"2013","unstructured":"De Matteis, L., Germani, R., Mancini, M. V., Savelli, G., Spreti, N., Brinchi, L., et al. (2013). Investigations to optimize the catalytic performance of CPO encapsulated in PEG 200-doped silica matrices. Journal of Molecular Catalysis B: Enzymatic, 97, 23\u201330.","journal-title":"Journal of Molecular Catalysis B: Enzymatic"},{"key":"2607_CR27","doi-asserted-by":"crossref","first-page":"2133","DOI":"10.1002\/adsc.200900303","volume":"351","author":"DI Perez","year":"2009","unstructured":"Perez, D. I., van Rantwijk, F., & Sheldon, R. A. (2009). Cross-linked enzyme aggregates of Chloroperoxidase: synthesis, optimization and characterization. Advanced Synthesis & Catalysis, 351, 2133\u20132139.","journal-title":"Advanced Synthesis & Catalysis"},{"key":"2607_CR28","doi-asserted-by":"crossref","first-page":"582","DOI":"10.1016\/j.enzmictec.2005.02.025","volume":"37","author":"CE Rotta Hernandez La","year":"2005","unstructured":"La Rotta Hernandez, C. E., L\u00fctz, S., Liese, A., & Bon, E. P. S. (2005). Activity and stability of Caldariomyces fumago chloroperoxidase modified by reductive alkylation, amidation and cross-linking. Enzyme and Microbial Technology, 37, 582\u2013588.","journal-title":"Enzyme and Microbial Technology"},{"key":"2607_CR29","doi-asserted-by":"crossref","first-page":"828","DOI":"10.1016\/S0006-291X(02)00766-0","volume":"295","author":"M Ayala","year":"2002","unstructured":"Ayala, M., Horjales, E., Pickard, M. A., & Vazquez-Duhalt, R. (2002). Cross-linked crystals of chloroperoxidase. Biochemical and Biophysical Research. Communications, 295, 828\u2013831.","journal-title":"Biochemical and Biophysical Research. Communications"},{"key":"2607_CR30","doi-asserted-by":"crossref","first-page":"1289","DOI":"10.1002\/adsc.200700082","volume":"349","author":"RA Sheldon","year":"2007","unstructured":"Sheldon, R. A. (2007). Enzyme immobilization: the quest for optimum performance. Advanced Synthesis & Catalysis, 349, 1289\u20131307.","journal-title":"Advanced Synthesis & Catalysis"},{"key":"2607_CR31","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/j.micromeso.2007.07.009","volume":"111","author":"MI Kim","year":"2008","unstructured":"Kim, M. I., Kim, J., Lee, J., Shin, S., Na, H. B., Hyeon, T., et al. (2008). One-dimensional crosslinked enzyme aggregates in SBA-15: superior catalytic behavior to conventional enzyme immobilization. Microporous and Mesoporous Materials, 111, 18\u201323.","journal-title":"Microporous and Mesoporous Materials"},{"key":"2607_CR32","doi-asserted-by":"crossref","first-page":"686","DOI":"10.1021\/cm991097v","volume":"12","author":"P Schmidt-Winkel","year":"2000","unstructured":"Schmidt-Winkel, P., Lukens, W. W., Yang, P., Margolese, D. I., Lettow, J. S., Ying, J. Y., et al. (2000). Microemulsion templating of siliceous mesostructured cellular foams with well-defined ultralarge mesopores. Chemistry of Materials, 12, 686\u2013696.","journal-title":"Chemistry of Materials"},{"key":"2607_CR33","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1002\/cssc.200800245","volume":"2","author":"D Jung","year":"2009","unstructured":"Jung, D., Paradiso, M., Wallacher, D., Brandt, A., & Hartmann, M. (2009). Formation of cross-linked chloroperoxidase aggregates in the pores of mesocellular foams: characterization by SANS and catalytic properties. Chem Sus Chem, 2, 161\u2013164.","journal-title":"Chem Sus Chem"},{"key":"2607_CR34","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/j.enzmictec.2014.04.014","volume":"61-62","author":"CY Shang","year":"2014","unstructured":"Shang, C. Y., Li, W. X., & Zhang, R. F. (2014). Immobilized Candida antarctica lipase B on ZnO nanowires\/macroporous silica composites for catalyzing chiral resolution of (RS)-2-octanol. Enzyme and Microbial Technology, 61-62, 28\u201334.","journal-title":"Enzyme and Microbial Technology"},{"key":"2607_CR35","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.molcatb.2014.12.016","volume":"113","author":"C-Y Shang","year":"2015","unstructured":"Shang, C.-Y., Li, W.-X., Jiang, F., & Zhang, R.-F. (2015). Improved enzymatic properties of Candida rugosa lipase immobilized on ZnO nanowires\/macroporous SiO2 microwave absorbing supports. Journal of Molecular Catalysis B: Enzymatic, 113, 9\u201313.","journal-title":"Journal of Molecular Catalysis B: Enzymatic"},{"key":"2607_CR36","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1016\/j.materresbull.2015.04.011","volume":"68","author":"C-Y Shang","year":"2015","unstructured":"Shang, C.-Y., Li, W.-X., & Zhang, R.-F. (2015). Immobilization of Candida rugosa lipase on ZnO nanowires\/macroporous silica composites for biocatalytic synthesis of phytosterol esters. Materials Research Bulletin, 68, 336\u2013342.","journal-title":"Materials Research Bulletin"},{"key":"2607_CR37","doi-asserted-by":"publisher","unstructured":"Sun H, Jin X, Jiang F, Zhang R. (2017). Immobilization of horseradish peroxidase on ZnO nanowires\/macroporous SiO2 composites for the complete decolorization of anthraquinone dyes. Biotechnology and Applied Biochemistry, n, \/a-n\/a. https:\/\/doi.org\/10.1002\/bab.1559 .","DOI":"10.1002\/bab.1559"},{"key":"2607_CR38","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.1016\/j.ijbiomac.2016.10.093","volume":"95","author":"H Sun","year":"2017","unstructured":"Sun, H., Jin, X., Long, N., & Zhang, R. (2017). Improved biodegradation of synthetic azo dye by horseradish peroxidase cross-linked on nano-composite support. International Journal of Biological Macromolecules, 95, 1049\u20131055.","journal-title":"International Journal of Biological Macromolecules"},{"key":"2607_CR39","doi-asserted-by":"crossref","first-page":"1763","DOI":"10.1016\/S0021-9258(18)96701-3","volume":"241","author":"DR Morris","year":"1966","unstructured":"Morris, D. R., & Hager, L. P. (1966). Chloroperoxidase: I. Isolation and properties of the crystalline glycoprotein. Journal of Biological Chemistry, 241, 1763\u20131768.","journal-title":"Journal of Biological Chemistry"},{"key":"2607_CR40","doi-asserted-by":"crossref","first-page":"1769","DOI":"10.1016\/S0021-9258(18)96702-5","volume":"241","author":"LP Hager","year":"1966","unstructured":"Hager, L. P., Morris, D. R., Brown, F. S., & Eberwein, H. (1966). Chloroperoxidase: II. Utilization of halogen anions. Journal of Biological Chemistry, 241, 1769\u20131777.","journal-title":"Journal of Biological Chemistry"},{"key":"2607_CR41","doi-asserted-by":"crossref","first-page":"6677","DOI":"10.1016\/j.tsf.2009.05.002","volume":"517","author":"R Zhang","year":"2009","unstructured":"Zhang, R., Long, N., & Zhang, L. (2009). Preparation of 3-dimensional SiO2 structures via a templating method. Thin Solid Films, 517, 6677\u20136680.","journal-title":"Thin Solid Films"},{"key":"2607_CR42","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","volume":"72","author":"MM Bradford","year":"1976","unstructured":"Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72, 248\u2013254.","journal-title":"Analytical Biochemistry"},{"key":"2607_CR43","doi-asserted-by":"crossref","first-page":"3129","DOI":"10.1016\/S0021-9258(18)63032-7","volume":"245","author":"JA Thomas","year":"1970","unstructured":"Thomas, J. A., Morris, D. R., & Hager, L. P. (1970). Chloroperoxidase: VII. Classical peroxidatic, catalatic, and halogenating forms of the enzyme. Journal of Biological Chemistry, 245, 3129\u20133134.","journal-title":"Journal of Biological Chemistry"},{"key":"2607_CR44","doi-asserted-by":"crossref","first-page":"891","DOI":"10.1016\/j.jhazmat.2010.11.091","volume":"186","author":"VK Gupta","year":"2011","unstructured":"Gupta, V. K., Gupta, B., Rastogi, A., Agarwal, S., & Nayak, A. (2011). A comparative investigation on adsorption performances of mesoporous activated carbon prepared from waste rubber tire and activated carbon for a hazardous azo dye\u2014acid blue 113. Journal of Hazardous Materials, 186, 891\u2013901.","journal-title":"Journal of Hazardous Materials"},{"key":"2607_CR45","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.jhazmat.2004.06.011","volume":"114","author":"M Isik","year":"2004","unstructured":"Isik, M., & Sponza, D. T. (2004). Monitoring of toxicity and intermediates of C.I. Direct black 38 azo dye through decolorization in an anaerobic\/aerobic sequential reactor system. Journal of Hazardous Materials, 114, 29\u201339.","journal-title":"Journal of Hazardous Materials"},{"key":"2607_CR46","doi-asserted-by":"crossref","first-page":"3647","DOI":"10.1016\/j.watres.2009.05.028","volume":"43","author":"KP Katuri","year":"2009","unstructured":"Katuri, K. P., Venkata Mohan, S., Sridhar, S., Pati, B. R., & Sarma, P. N. (2009). Laccase-membrane reactors for decolorization of an acid azo dye in aqueous phase: process optimization. Water Research, 43, 3647\u20133658.","journal-title":"Water Research"},{"key":"2607_CR47","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1007\/s10934-012-9608-8","volume":"20","author":"E Guerrero","year":"2013","unstructured":"Guerrero, E., Aburto, P., Terr\u00e9s, E., Villegas, O., Gonz\u00e1lez, E., Zayas, T., et al. (2013). Improvement of catalytic efficiency of chloroperoxidase by its covalent immobilization on SBA-15 for azo dye oxidation. Journal of Porous Materials, 20, 387\u2013396.","journal-title":"Journal of Porous Materials"},{"key":"2607_CR48","doi-asserted-by":"crossref","first-page":"995","DOI":"10.1016\/j.jhazmat.2009.01.077","volume":"167","author":"CC Hsueh","year":"2009","unstructured":"Hsueh, C. C., Chen, B. Y., & Yen, C. Y. (2009). Understanding effects of chemical structure on azo dye decolorization characteristics by Aeromonas hydrophila. Journal of Hazardous Materials, 167, 995\u20131001.","journal-title":"Journal of Hazardous Materials"},{"key":"2607_CR49","doi-asserted-by":"crossref","first-page":"12201","DOI":"10.1021\/ie5011492","volume":"53","author":"R Jiao","year":"2014","unstructured":"Jiao, R., Tan, Y., Jiang, Y., Hu, M., Li, S., & Zhai, Q. (2014). Ordered mesoporous silica matrix for immobilization of chloroperoxidase with enhanced biocatalytic performance for oxidative decolorization of azo dye. Industrial and Engineering Chemistry Research, 53, 12201\u201312208.","journal-title":"Industrial and Engineering Chemistry Research"}],"container-title":["Applied Biochemistry and Biotechnology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/article\/10.1007\/s12010-017-2607-0\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s12010-017-2607-0.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s12010-017-2607-0.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,8,3]],"date-time":"2022-08-03T01:55:16Z","timestamp":1659491716000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/s12010-017-2607-0"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,9,20]]},"references-count":49,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2018,3]]}},"alternative-id":["2607"],"URL":"https:\/\/doi.org\/10.1007\/s12010-017-2607-0","relation":{},"ISSN":["0273-2289","1559-0291"],"issn-type":[{"type":"print","value":"0273-2289"},{"type":"electronic","value":"1559-0291"}],"subject":[],"published":{"date-parts":[[2017,9,20]]}}}